Base de dados : MEDLINE
Pesquisa : D12.776.097.835 [Categoria DeCS]
Referências encontradas : 3792 [refinar]
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  1 / 3792 MEDLINE  
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[PMID]:29371614
[Au] Autor:Sreekanth KV; Sreejith S; Han S; Mishra A; Chen X; Sun H; Lim CT; Singh R
[Ad] Endereço:Division of Physics and Applied Physics, School of Physical and Mathematical Sciences, Nanyang Technological University, 21 Nanyang Link, Singapore, 637371, Singapore.
[Ti] Título:Biosensing with the singular phase of an ultrathin metal-dielectric nanophotonic cavity.
[So] Source:Nat Commun;9(1):369, 2018 01 25.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The concept of point of darkness has received much attention for biosensing based on phase-sensitive detection and perfect absorption of light. The maximum phase change is possible at the point of darkness where the reflection is almost zero. To date, this has been experimentally realized using different material systems through the concept of topological darkness. However, complex nanopatterning techniques are required to realize topological darkness. Here, we report an approach to realize perfect absorption and extreme phase singularity using a simple metal-dielectric multilayer thin-film stack. The multilayer stack works on the principle of an asymmetric Fabry-Perot cavity and shows an abrupt phase change at the reflectionless point due to the presence of a highly absorbing ultrathin film of germanium in the stack. In the proof-of-concept phase-sensitive biosensing experiments, we functionalize the film surface with an ultrathin layer of biotin-thiol to capture streptavidin at a low concentration of 1 pM.
[Mh] Termos MeSH primário: Técnicas Biossensoriais/métodos
Metais/química
[Mh] Termos MeSH secundário: Biotina/química
Estreptavidina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Metals); 6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180127
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-018-02860-6


  2 / 3792 MEDLINE  
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[PMID]:28470616
[Au] Autor:Gräslund S; Savitsky P; Müller-Knapp S
[Ad] Endereço:Structural Genomics Consortium, Department of Biochemistry and Biophysics, Karolinska Institutet, Tomtebodavägen 23a, Gamma:6, 171 65, Solna, Sweden. susanne.graslund@ki.se.
[Ti] Título:In Vivo Biotinylation of Antigens in E. coli.
[So] Source:Methods Mol Biol;1586:337-344, 2017.
[Is] ISSN:1940-6029
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Site-specific biotinylation of proteins is often the method of choice to enable efficient immobilization of a protein on a surface without interfering with protein folding. The tight interaction of biotin and streptavidin is frequently used to immobilize an antigen during phage display selections of binders. Here we describe a method of in vivo biotinylation of proteins during expression in E. coli, by tagging the protein with the short biotin acceptor peptide sequence, Avi tag, and co-expression of the E. coli biotin ligase (BirA) resulting in precise biotinylation of a specific lysine residue in the tag.
[Mh] Termos MeSH primário: Antígenos/química
Antígenos/genética
Escherichia coli/genética
Proteínas Imobilizadas/química
Proteínas Imobilizadas/genética
[Mh] Termos MeSH secundário: Animais
Biotina/química
Biotinilação
Carbono-Nitrogênio Ligases/química
Carbono-Nitrogênio Ligases/genética
Clonagem Molecular/métodos
Escherichia coli/química
Proteínas de Escherichia coli/química
Proteínas de Escherichia coli/genética
Expressão Gênica
Vetores Genéticos/genética
Seres Humanos
Proteínas Repressoras/química
Proteínas Repressoras/genética
Estreptavidina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens); 0 (Escherichia coli Proteins); 0 (Immobilized Proteins); 0 (Repressor Proteins); 6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin); EC 6.3.- (Carbon-Nitrogen Ligases); EC 6.3.4.15 (birA protein, E coli)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/978-1-4939-6887-9_22


  3 / 3792 MEDLINE  
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[PMID]:28461655
[Au] Autor:Mata J; Wise JA
[Ad] Endereço:Department of Biochemistry, University of Cambridge, Cambridge CB2 1QW, United Kingdom jm593@cam.ac.uk.
[Ti] Título:4-Thiouridine Labeling to Analyze mRNA Turnover in .
[So] Source:Cold Spring Harb Protoc;2017(5):pdb.prot091645, 2017 May 01.
[Is] ISSN:1559-6095
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Traditionally, the half-lives of mRNAs were measured after inhibition of transcription to allow decay of the preexisting population. The protocol presented here is a more recently developed strategy in which mRNA turnover is analyzed by measuring the decline in levels of newly synthesized RNA labeled with 4-thiouridine (4sU) during a brief pulse. After RNA extraction, the 4sU is biotinylated and the labeled species are purified using streptavidin beads. DNA microarrays can then be used to compare this population with total RNA, allowing half-lives to be calculated.
[Mh] Termos MeSH primário: Marcadores de Afinidade
RNA Fúngico/metabolismo
RNA Mensageiro/metabolismo
Schizosaccharomyces/metabolismo
Tiouridina
[Mh] Termos MeSH secundário: Antimetabólitos
Biotinilação
Meia-Vida
Indicadores e Reagentes
Análise de Sequência com Séries de Oligonucleotídeos
RNA Fúngico/biossíntese
RNA Mensageiro/análise
RNA Mensageiro/biossíntese
Estreptavidina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Affinity Labels); 0 (Antimetabolites); 0 (Indicators and Reagents); 0 (RNA, Fungal); 0 (RNA, Messenger); 13957-31-8 (Thiouridine); 9013-20-1 (Streptavidin)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180129
[Lr] Data última revisão:
180129
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE
[do] DOI:10.1101/pdb.prot091645


  4 / 3792 MEDLINE  
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[PMID]:29206886
[Au] Autor:Sedlak SM; Bauer MS; Kluger C; Schendel LC; Milles LF; Pippig DA; Gaub HE
[Ad] Endereço:Lehrstuhl für Angewandte Physik and Center for NanoScience (CeNS), Ludwig-Maximilians-Universität München, Munich, Germany.
[Ti] Título:Monodisperse measurement of the biotin-streptavidin interaction strength in a well-defined pulling geometry.
[So] Source:PLoS One;12(12):e0188722, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The widely used interaction of the homotetramer streptavidin with the small molecule biotin has been intensively studied by force spectroscopy and has become a model system for receptor ligand interaction. However, streptavidin's tetravalency results in diverse force propagation pathways through the different binding interfaces. This multiplicity gives rise to polydisperse force spectroscopy data. Here, we present an engineered monovalent streptavidin tetramer with a single cysteine in its functional subunit that allows for site-specific immobilization of the molecule, orthogonal to biotin binding. Functionality of streptavidin and its binding properties for biotin remain unaffected. We thus created a stable and reliable molecular anchor with a unique high-affinity binding site for biotinylated molecules or nanoparticles, which we expect to be useful for many single-molecule applications. To characterize the mechanical properties of the bond between biotin and our monovalent streptavidin, we performed force spectroscopy experiments using an atomic force microscope. We were able to conduct measurements at the single-molecule level with 1:1-stoichiometry and a well-defined geometry, in which force exclusively propagates through a single subunit of the streptavidin tetramer. For different force loading rates, we obtained narrow force distributions of the bond rupture forces ranging from 200 pN at 1,500 pN/s to 230 pN at 110,000 pN/s. The data are in very good agreement with the standard Bell-Evans model with a single potential barrier at Δx0 = 0.38 nm and a zero-force off-rate koff,0 in the 10-6 s-1 range.
[Mh] Termos MeSH primário: Biotina/química
Estreptavidina/química
[Mh] Termos MeSH secundário: Calorimetria
Cisteína/química
Eletroforese em Gel de Poliacrilamida
Microscopia de Força Atômica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171229
[Lr] Data última revisão:
171229
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171206
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188722


  5 / 3792 MEDLINE  
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[PMID]:28986262
[Au] Autor:Cheah JS; Yamada S
[Ad] Endereço:Biomedical Engineering Department, University of California, Davis, United States.
[Ti] Título:A simple elution strategy for biotinylated proteins bound to streptavidin conjugated beads using excess biotin and heat.
[So] Source:Biochem Biophys Res Commun;493(4):1522-1527, 2017 Dec 02.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Protein-protein interactions are the molecular basis of cell signaling. Recently, proximity based biotin identification (BioID) has emerged as an alternative approach to traditional co-immunoprecipitation. In this protocol, a mutant biotin ligase promiscuously labels proximal binding partners with biotin, and resulting biotinylated proteins are purified using streptavidin conjugated beads. This approach does not require preservation of protein complexes in vitro, making it an ideal approach to identify transient or weak protein complexes. However, due to the high affinity bond between streptavidin and biotin, elution of biotinylated proteins from streptavidin conjugated beads requires harsh denaturing conditions, which are often incompatible with downstream processing. To effectively release biotinylated proteins bound to streptavidin conjugated beads, we designed a series of experiments to determine optimal binding and elution conditions. Interestingly, the concentrations of SDS and IGEPAL-CA630 during the incubation with streptavidin conjugated beads were the key to effective elution of biotinylated proteins using excess biotin and heating. This protocol provides an alternative method to isolate biotinylated proteins from streptavidin conjugated beads that is suitable for further downstream analysis.
[Mh] Termos MeSH primário: Biotina/química
Proteínas/química
Proteínas/isolamento & purificação
[Mh] Termos MeSH secundário: Animais
Biotinilação
Western Blotting
Carbono-Nitrogênio Ligases/genética
Carbono-Nitrogênio Ligases/metabolismo
Cães
Eletroforese em Gel de Poliacrilamida
Proteínas de Escherichia coli/genética
Proteínas de Escherichia coli/metabolismo
Temperatura Alta
Imunoprecipitação
Células Madin Darby de Rim Canino
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
Solubilidade
Estreptavidina
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Proteins); 0 (Recombinant Proteins); 0 (Repressor Proteins); 6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin); EC 6.3.- (Carbon-Nitrogen Ligases); EC 6.3.4.15 (birA protein, E coli)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171121
[Lr] Data última revisão:
171121
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171008
[St] Status:MEDLINE


  6 / 3792 MEDLINE  
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[PMID]:28973477
[Au] Autor:Einarson OJ; Sen D
[Ad] Endereço:Department of Chemistry, Simon Fraser University, Burnaby, British Columbia V5A 1S6, Canada.
[Ti] Título:Self-biotinylation of DNA G-quadruplexes via intrinsic peroxidase activity.
[So] Source:Nucleic Acids Res;45(17):9813-9822, 2017 Sep 29.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The striking and ubiquitous in vitro affinity between hemin and DNA/RNA G-quadruplexes raises the intriguing possibility of its relevance to biology. To date, no satisfactory experimental framework has been reported for investigating such a possibility. Complexation by G-quadruplexes leads to activation of the bound hemin toward catalysis of 1- and 2-electron oxidative reactions, with phenolic compounds being particularly outstanding substrates. We report here a strategy for exploiting that intrinsic peroxidase activity of hemin•G-quadruplex complexes for self-biotinylation of their G-quadruplex component. Such self-biotinylation occurs with good efficiency and high discrimination in vitro, being specific for G-quadruplexes and not for duplexes. The biotinylated DNA, moreover, remains amenable to polymerase chain reaction amplification, rendering it suitable for analysis by ChIP-Seq and related methods. We anticipate that this self-biotinylation methodology will also serve as a sensitive tool, orthogonal to existing ones, for identifying, labeling and pulling down cellular RNA and DNA G-quadruplexes in general, as well as proteins bound to or proximal to such quadruplexes.
[Mh] Termos MeSH primário: DNA Catalítico/química
Quadruplex G
Hemina/química
Oligonucleotídeos/química
Peroxidases/química
[Mh] Termos MeSH secundário: Biocatálise
Técnicas Biossensoriais/métodos
Biotina/química
Biotinilação
Peróxido de Hidrogênio/química
Cinética
Mimetismo Molecular
Oxirredução
Fenóis/química
Reação em Cadeia da Polimerase
Estreptavidina/química
Tiramina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Catalytic); 0 (Oligonucleotides); 0 (Phenols); 0 (biotin tyramine); 6SO6U10H04 (Biotin); 743LRP9S7N (Hemin); 9013-20-1 (Streptavidin); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.- (Peroxidases); X8ZC7V0OX3 (Tyramine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171004
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkx765


  7 / 3792 MEDLINE  
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[PMID]:28966284
[Au] Autor:Chiba K; Hashimoto Y; Yamaguchi T
[Ad] Endereço:Institute of Molecular and Cellular Biosciences, The University of Tokyo.
[Ti] Título:Affinity Labeling with 4-Azidophthalimide (AzPI): Relation between Labeling Rate and Fluorescence Intensity.
[So] Source:Chem Pharm Bull (Tokyo);65(10):994-996, 2017.
[Is] ISSN:1347-5223
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:We recently developed 4-azidophthalimide (AzPI) as a compact fluorogenic photoreactive tag that can be attached to ligands to achieve selective fluorescence labeling of target proteins even in the presence of a large excess of non-target proteins. To further establish the utility of the AzPI tag, we focused here on streptavidin labeling with biotin-AzPI conjugates, and evaluated the relation between the amount of covalently labeled streptavidin (labeling rate) and fluorescence intensity. The labeling rate was proportional to the fluorescence intensity under standardized photo-irradiation conditions. Prolongation of the photo-irradiation time led to a marked increase in the labeling rate, but this was accompanied by a gradual decrease in the fluorescence intensity, which appeared to be due at least in part to photo-induced degradation of the target streptavidin. These findings should be helpful for achieving sensitive fluorescence detection of target proteins by using the AzPI tag.
[Mh] Termos MeSH primário: Corantes Fluorescentes/química
Ftalimidas/química
[Mh] Termos MeSH secundário: Marcadores de Afinidade
Biotina/química
Biotina/metabolismo
Células HEK293
Seres Humanos
Medições Luminescentes
Estreptavidina/química
Estreptavidina/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Affinity Labels); 0 (Fluorescent Dyes); 0 (Phthalimides); 1J6PQ7YI80 (phthalimide); 6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171030
[Lr] Data última revisão:
171030
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171003
[St] Status:MEDLINE
[do] DOI:10.1248/cpb.c17-00546


  8 / 3792 MEDLINE  
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[PMID]:28957393
[Au] Autor:Malaspina DC; Longo G; Szleifer I
[Ad] Endereço:Biomedical Engineering Department, Northwestern University, Evanston, Illinois, United States of America.
[Ti] Título:Behavior of ligand binding assays with crowded surfaces: Molecular model of antigen capture by antibody-conjugated nanoparticles.
[So] Source:PLoS One;12(9):e0185518, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ligand-receptor binding is of utmost importance in several biologically related disciplines. Ligand binding assays (LBA) use the high specificity and high affinity of ligands to detect, target or measure a specific receptors. One particular example of ligand binding assays are Antibody conjugated Nanoparticles (AcNPs), edge-cutting technologies that are present in several novel biomedical approaches for imaging, detection and treatment of diseases. However, the nano-confinement in AcNPs and LBA nanostructures introduces extra complexity in the analysis of ligand-receptor equilibriums. Because antibodies are large voluminous ligands, the effective affinity in AcNPs is often determined by antibody orientation and surface coverage. Moreover, antibodies have two binding sites introducing an extra ligand-receptor binding equilibrium. As consequence of all this, experimental or theoretical studies providing a guidelines for the prediction of the binding behavior in AcNPs are scarce. In this work, we present a set of theoretical calculations to shed light into the complex binding behavior of AcNPs and its implications in biomedical applications. To investigate the ligand-receptor binding on AcNPs, we have used a molecular theory that predicts the probability of different molecular conformations of the system depending on the local environment. We have considered two different pathways for designing these devices: covalently conjugated antibodies and streptavidin-biotin conjugated antibodies. We also explore the effects of surface coverage, bulk concentrations, nanoparticle size and antibody-antigen affinity. Overall, this work offers a series of theoretical predictions that can be used as a guide in the design of antibody conjugated nanoparticles for different applications.
[Mh] Termos MeSH primário: Anticorpos/metabolismo
Antígenos/metabolismo
Bioensaio/métodos
Modelos Moleculares
Nanopartículas/química
[Mh] Termos MeSH secundário: Biotina/metabolismo
Ligantes
Estreptavidina/metabolismo
Propriedades de Superfície
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies); 0 (Antigens); 0 (Ligands); 6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171019
[Lr] Data última revisão:
171019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170929
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185518


  9 / 3792 MEDLINE  
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[PMID]:28820961
[Au] Autor:Hytönen VP
[Ad] Endereço:Faculty of Medicine and Life Sciences and BioMediTech, University of Tampere, Lääkärinkatu 1, 33520 Tampere, Finland; Fimlab Laboratories, Biokatu 4, 33520 Tampere, Finland. Electronic address: vesa.hytonen@uta.fi.
[Ti] Título:Optimized Streptavidin for Fluorescent Labeling of Biotinylated Targets.
[So] Source:Cell Chem Biol;24(8):921-922, 2017 08 17.
[Is] ISSN:2451-9456
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In order to develop a streptavidin-biotin system with optimal performance in fluorescent labeling, in this issue of Cell Chemical Biology, Jacobsen et al. (2017) focused on changing the surface density of amino groups present on streptavidin via lysine mutagenesis. The streptavidin mutant containing only one free amino group was found superior to other streptavidin variants and was named Flavidin for fluorophore-friendly streptavidin.
[Mh] Termos MeSH primário: Biotinilação
Estreptavidina
[Mh] Termos MeSH secundário: Biotina
Corantes Fluorescentes
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
0 (Fluorescent Dyes); 6SO6U10H04 (Biotin); 9013-20-1 (Streptavidin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170819
[St] Status:MEDLINE


  10 / 3792 MEDLINE  
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[PMID]:28797844
[Au] Autor:Shi X; Zhang X; Li J; Zhao H; Mo L; Shi X; Hu Z; Gao J; Tan W
[Ad] Endereço:Department of Urology, Nanfang Hospital, Southern Medical University, Guangzhou, China.
[Ti] Título:PD-1/PD-L1 blockade enhances the efficacy of SA-GM-CSF surface-modified tumor vaccine in prostate cancer.
[So] Source:Cancer Lett;406:27-35, 2017 Oct 10.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Program death receptor-1 (PD-1)/program death ligand 1 (PD-L1) signaling plays an important role in tumor adaptive immune resistance. The streptavidin-granulocyte-macrophage colony stimulating factor (SA-GM-CSF) surface-modified tumor cells vaccine developed through our novel protein-anchor technology could significantly promote the activation of dendritic cells. Although GM-CSF vaccine could significantly increase the number of tumor-specific CD8 T-cells, the majority of these CD8 T-cells expressed PD-1. Moreover, GM-CSF vaccine up-regulated the PD-L1 expression of tumor cells, resulting in immune resistance. Adding PD-1/PD-L1 blockade to GM-CSF vaccine therapy could significantly increase the population of CD4 T, CD8 T and CD8 IFN-γ T but not CD4 Foxp3 T-cells and induced the highest production of IFN-γ. PD-1/PD-L1 blockade could effectively rescue the tumor-specific T lymphocytes generated by the GM-CSF vaccine, resulting in consistent tumor rejection. Taken together, PD-1/PD-L1 blockade combined with SA-GM-CSF-modified vaccine could effectively induce a strong specific antitumor immune response against prostate cancer.
[Mh] Termos MeSH primário: Antígeno B7-H1/antagonistas & inibidores
Vacinas Anticâncer/uso terapêutico
Fator Estimulador de Colônias de Granulócitos e Macrófagos/imunologia
Receptor de Morte Celular Programada 1/antagonistas & inibidores
Neoplasias da Próstata/terapia
Estreptavidina/química
[Mh] Termos MeSH secundário: Animais
Vacinas Anticâncer/imunologia
Linhagem Celular Tumoral
Progressão da Doença
Regulação Neoplásica da Expressão Gênica
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Neoplasias da Próstata/química
Neoplasias da Próstata/imunologia
Linfócitos T/imunologia
Linfócitos T Citotóxicos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (B7-H1 Antigen); 0 (Cancer Vaccines); 0 (Cd274 protein, mouse); 0 (Pdcd1 protein, mouse); 0 (Programmed Cell Death 1 Receptor); 83869-56-1 (Granulocyte-Macrophage Colony-Stimulating Factor); 9013-20-1 (Streptavidin)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE



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